Department of Cell Biology
Cell Line; Dystrophin; Humans; In Situ Hybridization, Fluorescence; Myosin Heavy Chains; Nuclear Proteins; RNA Precursors; RNA Processing, Post-Transcriptional; RNA Splicing; RNA, Messenger; *Ribonucleoproteins; Spliceosomes; Transcription, Genetic
Cell Biology | Life Sciences | Medicine and Health Sciences
Analysis of six endogenous pre-mRNAs demonstrates that localization at the periphery or within splicing factor-rich (SC-35) domains is not restricted to a few unusually abundant pre-mRNAs, but is apparently a more common paradigm of many protein-coding genes. Different genes are preferentially transcribed and their RNAs processed in different compartments relative to SC-35 domains. These differences do not simply correlate with the complexity, nuclear abundance, or position within overall nuclear space. The distribution of spliceosome assembly factor SC-35 did not simply mirror the distribution of individual pre-mRNAs, but rather suggested that individual domains contain both specific pre-mRNA(s) as well as excess splicing factors. This is consistent with a multifunctional compartment, to which some gene loci and their RNAs have access and others do not. Despite similar molar abundance in muscle fiber nuclei, nascent transcript "trees" of highly complex dystrophin RNA are cotranscriptionally spliced outside of SC-35 domains, whereas posttranscriptional "tracks" of more mature myosin heavy chain transcripts overlap domains. Further analyses supported that endogenous pre-mRNAs exhibit distinct structural organization that may reflect not only the expression and complexity of the gene, but also constraints of its chromosomal context and kinetics of its RNA metabolism.
Rights and Permissions
Citation: J Cell Biol. 1999 Feb 22;144(4):617-29. Link to article on publisher's website
DOI of Published Version
The Journal of cell biology
Smith, Kelly P.; Moen, Phillip T. Jr.; Wydner, Karen L.; Coleman, John R.; and Lawrence, Jeanne B., "Processing of endogenous pre-mRNAs in association with SC-35 domains is gene specific" (1999). Open Access Articles. 934.